node1 | node2 | node1 accession | node2 accession | node1 annotation | node2 annotation | score |
Bccel_0831 | Bccel_2586 | Bccel_0831 | Bccel_2586 | PFAM: peptidase S16 lon domain protein; KEGG: lon, Lon-A peptidase. | RNA-binding S4 domain protein; KEGG: ribosome-associated heat shock protein; PFAM: RNA-binding S4 domain protein; SMART: RNA-binding S4 domain protein. | 0.422 |
Bccel_0831 | Bccel_3709 | Bccel_0831 | Bccel_3709 | PFAM: peptidase S16 lon domain protein; KEGG: lon, Lon-A peptidase. | PFAM: heat shock protein Hsp90; KEGG: Heat shock protein Hsp90-like protein. | 0.765 |
Bccel_0831 | dnaJ | Bccel_0831 | Bccel_2058 | PFAM: peptidase S16 lon domain protein; KEGG: lon, Lon-A peptidase. | Chaperone protein dnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...] | 0.550 |
Bccel_0831 | groL | Bccel_0831 | Bccel_4027 | PFAM: peptidase S16 lon domain protein; KEGG: lon, Lon-A peptidase. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.703 |
Bccel_0831 | groL-2 | Bccel_0831 | Bccel_4373 | PFAM: peptidase S16 lon domain protein; KEGG: lon, Lon-A peptidase. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.703 |
Bccel_0831 | grpE | Bccel_0831 | Bccel_2060 | PFAM: peptidase S16 lon domain protein; KEGG: lon, Lon-A peptidase. | Protein grpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent i [...] | 0.790 |
Bccel_0831 | hslO | Bccel_0831 | Bccel_2612 | PFAM: peptidase S16 lon domain protein; KEGG: lon, Lon-A peptidase. | 33 kDa chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.616 |
Bccel_2586 | Bccel_0831 | Bccel_2586 | Bccel_0831 | RNA-binding S4 domain protein; KEGG: ribosome-associated heat shock protein; PFAM: RNA-binding S4 domain protein; SMART: RNA-binding S4 domain protein. | PFAM: peptidase S16 lon domain protein; KEGG: lon, Lon-A peptidase. | 0.422 |
Bccel_2586 | Bccel_3709 | Bccel_2586 | Bccel_3709 | RNA-binding S4 domain protein; KEGG: ribosome-associated heat shock protein; PFAM: RNA-binding S4 domain protein; SMART: RNA-binding S4 domain protein. | PFAM: heat shock protein Hsp90; KEGG: Heat shock protein Hsp90-like protein. | 0.577 |
Bccel_2586 | dnaJ | Bccel_2586 | Bccel_2058 | RNA-binding S4 domain protein; KEGG: ribosome-associated heat shock protein; PFAM: RNA-binding S4 domain protein; SMART: RNA-binding S4 domain protein. | Chaperone protein dnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...] | 0.468 |
Bccel_2586 | grpE | Bccel_2586 | Bccel_2060 | RNA-binding S4 domain protein; KEGG: ribosome-associated heat shock protein; PFAM: RNA-binding S4 domain protein; SMART: RNA-binding S4 domain protein. | Protein grpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent i [...] | 0.651 |
Bccel_2586 | hslO | Bccel_2586 | Bccel_2612 | RNA-binding S4 domain protein; KEGG: ribosome-associated heat shock protein; PFAM: RNA-binding S4 domain protein; SMART: RNA-binding S4 domain protein. | 33 kDa chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.873 |
Bccel_2586 | lon | Bccel_2586 | Bccel_2365 | RNA-binding S4 domain protein; KEGG: ribosome-associated heat shock protein; PFAM: RNA-binding S4 domain protein; SMART: RNA-binding S4 domain protein. | ATP-dependent protease La; ATP-dependent serine protease that mediates the selective degradation of mutant and abnormal proteins as well as certain short- lived regulatory proteins. Required for cellular homeostasis and for survival from DNA damage and developmental changes induced by stress. Degrades polypeptides processively to yield small peptide fragments that are 5 to 10 amino acids long. Binds to DNA in a double-stranded, site-specific manner. | 0.422 |
Bccel_2615 | hslO | Bccel_2615 | Bccel_2612 | KEGG: methyltransferase family protein. | 33 kDa chaperonin; Redox regulated molecular chaperone. Protects both thermally unfolding and oxidatively damaged proteins from irreversible aggregation. Plays an important role in the bacterial defense system toward oxidative stress. | 0.603 |
Bccel_3709 | Bccel_0831 | Bccel_3709 | Bccel_0831 | PFAM: heat shock protein Hsp90; KEGG: Heat shock protein Hsp90-like protein. | PFAM: peptidase S16 lon domain protein; KEGG: lon, Lon-A peptidase. | 0.765 |
Bccel_3709 | Bccel_2586 | Bccel_3709 | Bccel_2586 | PFAM: heat shock protein Hsp90; KEGG: Heat shock protein Hsp90-like protein. | RNA-binding S4 domain protein; KEGG: ribosome-associated heat shock protein; PFAM: RNA-binding S4 domain protein; SMART: RNA-binding S4 domain protein. | 0.577 |
Bccel_3709 | dnaJ | Bccel_3709 | Bccel_2058 | PFAM: heat shock protein Hsp90; KEGG: Heat shock protein Hsp90-like protein. | Chaperone protein dnaJ; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins and by disaggregating proteins, also in an autonomous, DnaK-independent fashion. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent interactions between DnaJ, D [...] | 0.984 |
Bccel_3709 | groL | Bccel_3709 | Bccel_4027 | PFAM: heat shock protein Hsp90; KEGG: Heat shock protein Hsp90-like protein. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.965 |
Bccel_3709 | groL-2 | Bccel_3709 | Bccel_4373 | PFAM: heat shock protein Hsp90; KEGG: Heat shock protein Hsp90-like protein. | 60 kDa chaperonin; Prevents misfolding and promotes the refolding and proper assembly of unfolded polypeptides generated under stress conditions. | 0.965 |
Bccel_3709 | grpE | Bccel_3709 | Bccel_2060 | PFAM: heat shock protein Hsp90; KEGG: Heat shock protein Hsp90-like protein. | Protein grpE; Participates actively in the response to hyperosmotic and heat shock by preventing the aggregation of stress-denatured proteins, in association with DnaK and GrpE. It is the nucleotide exchange factor for DnaK and may function as a thermosensor. Unfolded proteins bind initially to DnaJ; upon interaction with the DnaJ-bound protein, DnaK hydrolyzes its bound ATP, resulting in the formation of a stable complex. GrpE releases ADP from DnaK; ATP binding to DnaK triggers the release of the substrate protein, thus completing the reaction cycle. Several rounds of ATP-dependent i [...] | 0.915 |